ID A0A261QKF0_9BACI Unreviewed; 570 AA.
AC A0A261QKF0;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 27-MAR-2024, entry version 14.
DE RecName: Full=Rqc2 homolog RqcH {ECO:0000256|HAMAP-Rule:MF_00844};
DE Short=RqcH {ECO:0000256|HAMAP-Rule:MF_00844};
GN Name=rqcH {ECO:0000256|HAMAP-Rule:MF_00844};
GN ORFNames=CEW92_02150 {ECO:0000313|EMBL:OZI13289.1};
OS Bacillaceae bacterium SAS-127.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae.
OX NCBI_TaxID=2015203 {ECO:0000313|EMBL:OZI13289.1, ECO:0000313|Proteomes:UP000217062};
RN [1] {ECO:0000313|EMBL:OZI13289.1, ECO:0000313|Proteomes:UP000217062}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SAS-127 {ECO:0000313|EMBL:OZI13289.1,
RC ECO:0000313|Proteomes:UP000217062};
RA Verma A., Pal Y., Krishnamurthi S.;
RT "Indiibacillus sp. (SAS-127) genome sequencing.";
RL Submitted (JUN-2017) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Part of the ribosome quality control system (RQC). Recruits
CC Ala-charged tRNA and directs the elongation of stalled nascent chains
CC on 50S ribosomal subunits, leading to non-templated C-terminal Ala
CC extensions (Ala tail). The Ala tail promotes nascent chain degradation.
CC May add between 1 and at least 8 Ala residues. Binds to stalled 50S
CC ribosomal subunits. {ECO:0000256|HAMAP-Rule:MF_00844}.
CC -!- SUBUNIT: Associates with stalled 50S ribosomal subunits.
CC {ECO:0000256|HAMAP-Rule:MF_00844}.
CC -!- SIMILARITY: Belongs to the NEMF family. {ECO:0000256|HAMAP-
CC Rule:MF_00844}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:OZI13289.1}.
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DR EMBL; NKXN01000008; OZI13289.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A261QKF0; -.
DR OrthoDB; 9766163at2; -.
DR Proteomes; UP000217062; Unassembled WGS sequence.
DR GO; GO:0043023; F:ribosomal large subunit binding; IEA:UniProtKB-UniRule.
DR GO; GO:0000049; F:tRNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0072344; P:rescue of stalled ribosome; IEA:UniProtKB-UniRule.
DR Gene3D; 1.10.8.50; -; 1.
DR Gene3D; 3.40.970.40; fibrinogen binding protein from staphylococcus aureus domain like; 1.
DR Gene3D; 2.30.310.10; ibrinogen binding protein from staphylococcus aureus domain; 1.
DR HAMAP; MF_00844_B; RqcH_B; 1.
DR InterPro; IPR008532; NFACT_RNA-bd.
DR InterPro; IPR043682; RqcH_bacterial.
DR PANTHER; PTHR15239; NUCLEAR EXPORT MEDIATOR FACTOR NEMF; 1.
DR PANTHER; PTHR15239:SF6; RIBOSOME QUALITY CONTROL COMPLEX SUBUNIT NEMF; 1.
DR Pfam; PF05670; NFACT-R_1; 1.
DR Pfam; PF18297; NFACT-R_2; 1.
DR Pfam; PF05833; NFACT_N; 1.
PE 3: Inferred from homology;
KW Coiled coil {ECO:0000256|HAMAP-Rule:MF_00844};
KW Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917, ECO:0000256|HAMAP-
KW Rule:MF_00844}; Reference proteome {ECO:0000313|Proteomes:UP000217062};
KW RNA-binding {ECO:0000256|ARBA:ARBA00022884, ECO:0000256|HAMAP-
KW Rule:MF_00844};
KW tRNA-binding {ECO:0000256|ARBA:ARBA00022555, ECO:0000256|HAMAP-
KW Rule:MF_00844}.
FT DOMAIN 451..540
FT /note="NFACT RNA-binding"
FT /evidence="ECO:0000259|Pfam:PF05670"
FT COILED 284..322
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00844"
SQ SEQUENCE 570 AA; 64998 MW; AF0B341024031237 CRC64;
MSFDGLFTRA ITKELLEQLQ GGRVNKIHQP YKNETVLVIR AKGGNHKLLL SAHPSYARVQ
LTSEAYENPQ EPPLFCMMMR KHLEGAVLEN IQQVGLDRLL IFEFKGKNEI GDISYKQLFV
EIMGRHSNIV LVDKQKGTII DSIKHISAAV NSYRSILPGY EYIAPPEQHK ANPLEADTEE
VLRKIDFNSG RLDRQLVSNF AGLSPLIAKE IISTCGMANR DTLPSAFVNE MSTIKQHQYT
PTFIEQEQKS FFYMKDLSHL EGERKTFATL SELLDRYYVG KAARDRVKQQ ANDLERFIKN
EKEKNETKLG KLHRTLQEAE NADQFQLMGE LLTAHLYAVE KGMTEIEVVN YYDEEGGKIT
IALDPRKTPS ENAQKYFSKY QKAKNAILVV KEQIDKTNEE ILYFDNLLQQ LESASPKDIE
EIREELAEEG YIKLKATKKK KPANKKPDIE TFTASDGTLL FVGKNNKQND YLTNKFARRD
EIWLHTKDIP GSHVVIRSEE PSEQTILEAA NLAAYFSKAK ESSSVPVDFT KVRHVKKPNG
AKPGFVIYDN QQTVYVTPNE DLVLKMKGVK
//
